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Q16602

- CALRL_HUMAN

UniProt

Q16602 - CALRL_HUMAN

Protein

Calcitonin gene-related peptide type 1 receptor

Gene

CALCRL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 2 (14 Apr 2009)
      Previous versions | rss
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    Functioni

    Receptor for calcitonin-gene-related peptide (CGRP) together with RAMP1 and receptor for adrenomedullin together with RAMP3 By similarity. Receptor for adrenomedullin together with RAMP2. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.By similarity1 Publication

    GO - Molecular functioni

    1. adrenomedullin receptor activity Source: UniProtKB
    2. calcitonin gene-related peptide receptor activity Source: Ensembl
    3. calcitonin receptor activity Source: Ensembl
    4. G-protein coupled receptor activity Source: ProtInc
    5. protein binding Source: UniProtKB
    6. protein transporter activity Source: UniProtKB

    GO - Biological processi

    1. adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: Ensembl
    2. angiogenesis Source: UniProtKB
    3. calcium ion transport Source: UniProtKB
    4. cAMP biosynthetic process Source: UniProtKB
    5. cellular response to sucrose stimulus Source: UniProtKB
    6. G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger Source: ProtInc
    7. heart development Source: Ensembl
    8. negative regulation of inflammatory response Source: Ensembl
    9. positive regulation of cAMP biosynthetic process Source: UniProtKB
    10. positive regulation of smooth muscle cell proliferation Source: Ensembl
    11. protein transport Source: UniProtKB
    12. receptor internalization Source: UniProtKB
    13. regulation of muscle contraction Source: Ensembl

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Enzyme and pathway databases

    ReactomeiREACT_18290. Calcitonin-like ligand receptors.
    REACT_19327. G alpha (s) signalling events.

    Protein family/group databases

    TCDBi9.A.14.4.12. the g-protein-coupled receptor (gpcr) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calcitonin gene-related peptide type 1 receptor
    Short name:
    CGRP type 1 receptor
    Alternative name(s):
    Calcitonin receptor-like receptor
    Gene namesi
    Name:CALCRL
    Synonyms:CGRPR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:16709. CALCRL.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. endosome Source: UniProtKB
    3. integral component of plasma membrane Source: ProtInc
    4. lysosome Source: UniProtKB
    5. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi72 – 721W → A: Strongly reduced affinity for adrenomedullin. 1 Publication
    Mutagenesisi92 – 921F → A: Strongly reduced affinity for adrenomedullin. 1 Publication
    Mutagenesisi121 – 1211W → A: Strongly reduced affinity for adrenomedullin. 1 Publication

    Organism-specific databases

    PharmGKBiPA26033.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 22221 PublicationAdd
    BLAST
    Chaini23 – 461439Calcitonin gene-related peptide type 1 receptorPRO_0000012811Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi48 ↔ 74
    Disulfide bondi65 ↔ 105
    Glycosylationi66 – 661N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi88 ↔ 127
    Glycosylationi118 – 1181N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi123 – 1231N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ16602.
    PRIDEiQ16602.

    PTM databases

    PhosphoSiteiQ16602.

    Expressioni

    Tissue specificityi

    Predominantly expressed in the lung and heart.

    Gene expression databases

    ArrayExpressiQ16602.
    BgeeiQ16602.
    CleanExiHS_CALCRL.
    GenevestigatoriQ16602.

    Organism-specific databases

    HPAiHPA008070.

    Interactioni

    Subunit structurei

    Heterodimer of CALCRL and RAMP3 By similarity. Heterodimer of CALCRL and RAMP1 or CALCRL and RAMP2.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CALCAP068812EBI-962878,EBI-962928

    Protein-protein interaction databases

    BioGridi115498. 4 interactions.
    DIPiDIP-37674N.
    IntActiQ16602. 2 interactions.
    STRINGi9606.ENSP00000376177.

    Structurei

    Secondary structure

    1
    461
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi33 – 5220
    Beta strandi63 – 653
    Beta strandi83 – 875
    Beta strandi90 – 923
    Beta strandi99 – 1057
    Turni115 – 1173
    Helixi125 – 1273
    Helixi129 – 1313

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3AQFX-ray2.60B23-136[»]
    3N7PX-ray2.80A/B/C/J23-133[»]
    3N7RX-ray2.90A/B23-133[»]
    3N7SX-ray2.10A/B23-133[»]
    ProteinModelPortaliQ16602.
    SMRiQ16602. Positions 36-132, 140-388.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16602.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 146124ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini167 – 1737CytoplasmicSequence Analysis
    Topological domaini194 – 21320ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini237 – 25317CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini274 – 28916ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini314 – 33623CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini355 – 36612ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini389 – 46173CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei147 – 16620Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei174 – 19320Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei214 – 23623Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei254 – 27320Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei290 – 31324Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei337 – 35418Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei367 – 38822Helical; Name=7Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG255868.
    HOVERGENiHBG102129.
    InParanoidiQ16602.
    KOiK04577.
    OMAiLCWNDVA.
    OrthoDBiEOG712TW2.
    PhylomeDBiQ16602.
    TreeFamiTF315710.

    Family and domain databases

    InterProiIPR003287. GCPR_2_calcitonin_rcpt_fam.
    IPR017981. GPCR_2-like.
    IPR003289. GPCR_2_CGRP1_rcpt.
    IPR001879. GPCR_2_extracellular_dom.
    IPR000832. GPCR_2_secretin-like.
    IPR017983. GPCR_2_secretin-like_CS.
    [Graphical view]
    PfamiPF00002. 7tm_2. 1 hit.
    PF02793. HRM. 1 hit.
    [Graphical view]
    PRINTSiPR01351. CGRPRECEPTOR.
    PR01350. CTRFAMILY.
    PR00249. GPCRSECRETIN.
    SMARTiSM00008. HormR. 1 hit.
    [Graphical view]
    PROSITEiPS00649. G_PROTEIN_RECEP_F2_1. 1 hit.
    PS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
    PS50227. G_PROTEIN_RECEP_F2_3. 1 hit.
    PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q16602-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEKKCTLNFL VLLPFFMILV TAELEESPED SIQLGVTRNK IMTAQYECYQ    50
    KIMQDPIQQA EGVYCNRTWD GWLCWNDVAA GTESMQLCPD YFQDFDPSEK 100
    VTKICDQDGN WFRHPASNRT WTNYTQCNVN THEKVKTALN LFYLTIIGHG 150
    LSIASLLISL GIFFYFKSLS CQRITLHKNL FFSFVCNSVV TIIHLTAVAN 200
    NQALVATNPV SCKVSQFIHL YLMGCNYFWM LCEGIYLHTL IVVAVFAEKQ 250
    HLMWYYFLGW GFPLIPACIH AIARSLYYND NCWISSDTHL LYIIHGPICA 300
    ALLVNLFFLL NIVRVLITKL KVTHQAESNL YMKAVRATLI LVPLLGIEFV 350
    LIPWRPEGKI AEEVYDYIMH ILMHFQGLLV STIFCFFNGE VQAILRRNWN 400
    QYKIQFGNSF SNSEALRSAS YTVSTISDGP GYSHDCPSEH LNGKSIHDIE 450
    NVLLKPENLY N 461
    Length:461
    Mass (Da):52,929
    Last modified:April 14, 2009 - v2
    Checksum:iAF98E55E5454767C
    GO

    Sequence cautioni

    The sequence BAF84319.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti144 – 1441L → Q in BAF84319. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti8 – 81N → Y.1 Publication
    Corresponds to variant rs698577 [ dbSNP | Ensembl ].
    VAR_054822
    Natural varianti16 – 161F → L.
    Corresponds to variant rs13391909 [ dbSNP | Ensembl ].
    VAR_049453
    Natural varianti274 – 2741R → I.
    Corresponds to variant rs34010553 [ dbSNP | Ensembl ].
    VAR_049454

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L76380 mRNA. Translation: AAC41994.1.
    U17473 mRNA. Translation: AAA62158.1.
    AY389506 mRNA. Translation: AAQ91332.1.
    AK291630 mRNA. Translation: BAF84319.1. Different initiation.
    AK292998 mRNA. Translation: BAF85687.1.
    AC007319 Genomic DNA. Translation: AAY14806.1.
    AC074020 Genomic DNA. Translation: AAY14996.1.
    CCDSiCCDS2293.1.
    PIRiJC2477.
    RefSeqiNP_001258680.1. NM_001271751.1.
    NP_005786.1. NM_005795.5.
    UniGeneiHs.470882.
    Hs.744587.

    Genome annotation databases

    EnsembliENST00000392370; ENSP00000376177; ENSG00000064989.
    ENST00000409998; ENSP00000386972; ENSG00000064989.
    ENST00000410068; ENSP00000387190; ENSG00000064989.
    GeneIDi10203.
    KEGGihsa:10203.

    Polymorphism databases

    DMDMi226693507.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L76380 mRNA. Translation: AAC41994.1 .
    U17473 mRNA. Translation: AAA62158.1 .
    AY389506 mRNA. Translation: AAQ91332.1 .
    AK291630 mRNA. Translation: BAF84319.1 . Different initiation.
    AK292998 mRNA. Translation: BAF85687.1 .
    AC007319 Genomic DNA. Translation: AAY14806.1 .
    AC074020 Genomic DNA. Translation: AAY14996.1 .
    CCDSi CCDS2293.1.
    PIRi JC2477.
    RefSeqi NP_001258680.1. NM_001271751.1.
    NP_005786.1. NM_005795.5.
    UniGenei Hs.470882.
    Hs.744587.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3AQF X-ray 2.60 B 23-136 [» ]
    3N7P X-ray 2.80 A/B/C/J 23-133 [» ]
    3N7R X-ray 2.90 A/B 23-133 [» ]
    3N7S X-ray 2.10 A/B 23-133 [» ]
    ProteinModelPortali Q16602.
    SMRi Q16602. Positions 36-132, 140-388.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115498. 4 interactions.
    DIPi DIP-37674N.
    IntActi Q16602. 2 interactions.
    STRINGi 9606.ENSP00000376177.

    Chemistry

    BindingDBi Q16602.
    ChEMBLi CHEMBL2111191.

    Protein family/group databases

    TCDBi 9.A.14.4.12. the g-protein-coupled receptor (gpcr) family.
    GPCRDBi Search...

    PTM databases

    PhosphoSitei Q16602.

    Polymorphism databases

    DMDMi 226693507.

    Proteomic databases

    PaxDbi Q16602.
    PRIDEi Q16602.

    Protocols and materials databases

    DNASUi 10203.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000392370 ; ENSP00000376177 ; ENSG00000064989 .
    ENST00000409998 ; ENSP00000386972 ; ENSG00000064989 .
    ENST00000410068 ; ENSP00000387190 ; ENSG00000064989 .
    GeneIDi 10203.
    KEGGi hsa:10203.

    Organism-specific databases

    CTDi 10203.
    GeneCardsi GC02M188171.
    HGNCi HGNC:16709. CALCRL.
    HPAi HPA008070.
    MIMi 114190. gene.
    neXtProti NX_Q16602.
    PharmGKBi PA26033.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG255868.
    HOVERGENi HBG102129.
    InParanoidi Q16602.
    KOi K04577.
    OMAi LCWNDVA.
    OrthoDBi EOG712TW2.
    PhylomeDBi Q16602.
    TreeFami TF315710.

    Enzyme and pathway databases

    Reactomei REACT_18290. Calcitonin-like ligand receptors.
    REACT_19327. G alpha (s) signalling events.

    Miscellaneous databases

    EvolutionaryTracei Q16602.
    GeneWikii CALCRL.
    GenomeRNAii 10203.
    NextBioi 38620.
    PROi Q16602.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16602.
    Bgeei Q16602.
    CleanExi HS_CALCRL.
    Genevestigatori Q16602.

    Family and domain databases

    InterProi IPR003287. GCPR_2_calcitonin_rcpt_fam.
    IPR017981. GPCR_2-like.
    IPR003289. GPCR_2_CGRP1_rcpt.
    IPR001879. GPCR_2_extracellular_dom.
    IPR000832. GPCR_2_secretin-like.
    IPR017983. GPCR_2_secretin-like_CS.
    [Graphical view ]
    Pfami PF00002. 7tm_2. 1 hit.
    PF02793. HRM. 1 hit.
    [Graphical view ]
    PRINTSi PR01351. CGRPRECEPTOR.
    PR01350. CTRFAMILY.
    PR00249. GPCRSECRETIN.
    SMARTi SM00008. HormR. 1 hit.
    [Graphical view ]
    PROSITEi PS00649. G_PROTEIN_RECEP_F2_1. 1 hit.
    PS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
    PS50227. G_PROTEIN_RECEP_F2_3. 1 hit.
    PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A cDNA encoding the calcitonin gene-related peptide type 1 receptor."
      Aiyar N., Rand K., Elshourbagy N.A., Zeng Z., Adamou J.E., Bergsma D.J., Li Y.
      J. Biol. Chem. 271:11325-11329(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lung.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Cerebellum.
    3. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
      Kopatz S.A., Aronstam R.S., Sharma S.V.
      Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Heart.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT TYR-8.
      Tissue: Placenta and Trachea.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 23-37.
    7. "Crystal structure of the ectodomain complex of the CGRP receptor, a class-B GPCR, reveals the site of drug antagonism."
      ter Haar E., Koth C.M., Abdul-Manan N., Swenson L., Coll J.T., Lippke J.A., Lepre C.A., Garcia-Guzman M., Moore J.M.
      Structure 18:1083-1093(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 23-133 IN COMPLEX WITH RAMP1 AND ANTAGONIST, SUBUNIT, DISULFIDE BONDS.
    8. "Structural basis for extracellular interactions between calcitonin receptor-like receptor and receptor activity-modifying protein 2 for adrenomedullin-specific binding."
      Kusano S., Kukimoto-Niino M., Hino N., Ohsawa N., Okuda K., Sakamoto K., Shirouzu M., Shindo T., Yokoyama S.
      Protein Sci. 21:199-210(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 23-136 IN COMPLEX WITH RAMP2, FUNCTION, MUTAGENESIS OF TRP-72; PHE-92 AND TRP-121, DISULFIDE BONDS.

    Entry informationi

    Entry nameiCALRL_HUMAN
    AccessioniPrimary (citable) accession number: Q16602
    Secondary accession number(s): A8K6G5
    , A8KAD3, Q53S02, Q53TS5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: April 14, 2009
    Last modified: October 1, 2014
    This is version 135 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3